6dgn

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<StructureSection load='6dgn' size='340' side='right'caption='[[6dgn]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='6dgn' size='340' side='right'caption='[[6dgn]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6dgn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_cenocepacia_pc184 Burkholderia cenocepacia pc184] and [http://en.wikipedia.org/wiki/Crotz Crotz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DGN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DGN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6dgn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_cenocepacia_PC184 Burkholderia cenocepacia PC184] and [https://en.wikipedia.org/wiki/Cronobacter_turicensis_z3032 Cronobacter turicensis z3032]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DGN FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.999&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BCPG_03941 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=350702 Burkholderia cenocepacia PC184]), gmr, Ctu_23300 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=693216 CROTZ])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6dgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dgn OCA], [http://pdbe.org/6dgn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dgn RCSB], [http://www.ebi.ac.uk/pdbsum/6dgn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dgn ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6dgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dgn OCA], [https://pdbe.org/6dgn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dgn RCSB], [https://www.ebi.ac.uk/pdbsum/6dgn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dgn ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A2W0S6_9BURK A2W0S6_9BURK]
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The diffusible signal factors (DSFs) are a family of quorum-sensing autoinducers (AIs) produced and detected by numerous gram-negative bacteria. The DSF family AIs are fatty acids, differing in their acyl chain length, branching, and substitution but having in common a cis-2 double bond that is required for their activity. In both human and plant pathogens, DSFs regulate diverse phenotypes, including virulence factor expression, antibiotic resistance, and biofilm dispersal. Despite their widespread relevance to both human health and agriculture, the molecular basis of DSF recognition by their cellular receptors remained a mystery. Here, we report the first structure-function studies of the DSF receptor regulation of pathogenicity factor R (RpfR). We present the X-ray crystal structure of the RpfR DSF-binding domain in complex with the Burkholderia DSF (BDSF), which to our knowledge is the first structure of a DSF receptor in complex with its AI. To begin to understand the mechanistic role of the BDSF-RpfR contacts observed in the biologically important complex, we have also determined the X-ray crystal structure of the RpfR DSF-binding domain in complex with the inactive, saturated isomer of BDSF, dodecanoic acid (C12:0). In addition to these ligand-receptor complex structures, we report the discovery of a previously overlooked RpfR domain and show that it binds to and negatively regulates the DSF synthase regulation of pathogenicity factor F (RpfF). We have named this RpfR region the RpfF interaction (FI) domain, and we have determined its X-ray crystal structure alone and in complex with RpfF. These X-ray crystal structures, together with extensive complementary in vivo and in vitro functional studies, reveal the molecular basis of DSF recognition and the importance of the cis-2 double bond to DSF function. Finally, we show that throughout cellular growth, the production of BDSF by RpfF is post-translationally controlled by the RpfR N-terminal FI domain, affecting the cellular concentration of the bacterial second messenger bis-(3'-5')-cyclic dimeric guanosine monophosphate (c-di-GMP). Thus, in addition to describing the molecular basis for the binding and specificity of a DSF for its receptor, we describe a receptor-synthase interaction regulating bacterial quorum-sensing signaling and second messenger signal transduction.
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Structural basis of DSF recognition by its receptor RpfR and its regulatory interaction with the DSF synthase RpfF.,Waldron EJ, Snyder D, Fernandez NL, Sileo E, Inoyama D, Freundlich JS, Waters CM, Cooper VS, Neiditch MB PLoS Biol. 2019 Feb 4;17(2):e3000123. doi: 10.1371/journal.pbio.3000123., eCollection 2019 Feb. PMID:30716063<ref>PMID:30716063</ref>
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==See Also==
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*[[Enoyl-CoA hydratase 3D structures|Enoyl-CoA hydratase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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*[[Nonstructural protein 3D structures|Nonstructural protein 3D structures]]
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</div>
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<div class="pdbe-citations 6dgn" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Burkholderia cenocepacia pc184]]
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[[Category: Burkholderia cenocepacia PC184]]
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[[Category: Crotz]]
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[[Category: Cronobacter turicensis z3032]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Neiditch, M B]]
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[[Category: Neiditch MB]]
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[[Category: Waldron, E J]]
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[[Category: Waldron EJ]]
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[[Category: Diffusible signal factor]]
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[[Category: Diguanylate cyclase]]
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[[Category: Phosphodiesterase]]
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[[Category: Quorum sensing]]
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[[Category: Unknown function]]
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Current revision

Cronobacter turicensis BDSF synthase RpfF in complex with the RpfR quorum-sensing receptor FI domain

PDB ID 6dgn

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